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Database: UniProt
Entry: Q8EX97
LinkDB: Q8EX97
Original site: Q8EX97 
ID   ALR_LEPIN               Reviewed;         389 AA.
AC   Q8EX97;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 100.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=LB_317;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai
OS   (strain 56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AE010301; AAN51876.1; -; Genomic_DNA.
DR   RefSeq; NP_714861.1; NC_004343.2.
DR   RefSeq; WP_001152323.1; NC_004343.2.
DR   ProteinModelPortal; Q8EX97; -.
DR   SMR; Q8EX97; -.
DR   STRING; 189518.LB_317; -.
DR   PRIDE; Q8EX97; -.
DR   EnsemblBacteria; AAN51876; AAN51876; LB_317.
DR   GeneID; 1153876; -.
DR   KEGG; lil:LB_317; -.
DR   PATRIC; fig|189518.3.peg.4636; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; Q8EX97; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   BioCyc; LINT189518:G1GL4-3701-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001408; Chromosome II.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    389       Alanine racemase.
FT                                /FTId=PRO_0000114531.
FT   ACT_SITE     48     48       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    281    281       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     144    144       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     329    329       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   389 AA;  43278 MW;  B44569674B85B3BF CRC64;
     MQDINSGSSS MKDTYSSWIE ISKRSLSNNL DNFRSILRPN STLTAILKSN AYGHGIEPMT
     RLCIEAGISR IGVNSIEEAL LIRNIDSKIP ILIMGEIQNP EKRKDVLSDP NFWIVFSRPE
     TARILSSFLP APKLHLKIDT GMGRLGSHGE TLKQTLSELK NVGITLGGIC THFASTEDVL
     EHKYSLMQTQ KFEEAIFLAK SFGYNHLIRH ACASASTMLF PNAHFDMVRI GISLYGLWPS
     IQTRLSLNLT GNKNFQLNPI LSWKSRIVHI QYHPADSYIG YGSTFQTSYP TKVAIVPVGY
     YEGLDRKLSS NGDMLVLGKK ARIIGRICMN MTMLDVTHIP GAEVGSIVTI IGQDGEESIT
     ADDLADRTHT INYEVMTRIS ESIPRIVVD
//
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